2003
DOI: 10.1073/pnas.1333907100
|View full text |Cite
|
Sign up to set email alerts
|

Rapid amyloid fiber formation from the fast-folding WW domain FBP28

Abstract: The WW domains are small proteins that contain a three-stranded, antiparallel ␤-sheet. The 40-residue murine FBP28 WW domain rapidly formed twirling ribbon-like fibrils at physiological temperature and pH, with morphology typical of amyloid fibrils. These ribbons were unusually wide and well ordered, making them highly suitable for structural studies. Their x-ray and electrondiffraction patterns displayed the characteristic amyloid fiber 0.47-nm reflection of the cross-␤ diffraction signature. Both conventiona… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

8
87
0
2

Year Published

2004
2004
2015
2015

Publication Types

Select...
5
2

Relationship

0
7

Authors

Journals

citations
Cited by 83 publications
(97 citation statements)
references
References 41 publications
8
87
0
2
Order By: Relevance
“…4. In agreement with numerous experiments, [17][18][19][20][21][22][23][24][25][26] the fibril growth exhibits the characteristic sigmoidal curve which can be divided into three stages: ͑1͒ nucleation stage, where the fibril grows and redissolves back and forth until its size exceeds a critical nucleus size, i.e., R Ͼ R c ; ͑2͒ growth stage, where R is found to increase linearly with time; and ͑3͒ equilibrium stage, where R reaches a plateau as the free peptides in the simulation box are exhausted. The duration of the nucleation stage, called "lag time" , can be obtained from the R-t curves.…”
Section: Fibril Size and Lag Timesupporting
confidence: 91%
See 3 more Smart Citations
“…4. In agreement with numerous experiments, [17][18][19][20][21][22][23][24][25][26] the fibril growth exhibits the characteristic sigmoidal curve which can be divided into three stages: ͑1͒ nucleation stage, where the fibril grows and redissolves back and forth until its size exceeds a critical nucleus size, i.e., R Ͼ R c ; ͑2͒ growth stage, where R is found to increase linearly with time; and ͑3͒ equilibrium stage, where R reaches a plateau as the free peptides in the simulation box are exhausted. The duration of the nucleation stage, called "lag time" , can be obtained from the R-t curves.…”
Section: Fibril Size and Lag Timesupporting
confidence: 91%
“…48 Our model can naturally apply to the case of flat-ribbonlike amyloid fibrils, 19,22,[49][50][51] with possible extension to twisted ribbons 6,24,35,[50][51][52] or coiled helical structure with constant interacting regions ͓Fig. 6͑a͒ of Ref.…”
Section: Model and Simulation Algorithmmentioning
confidence: 99%
See 2 more Smart Citations
“…1N), has been shown to fold with biphasic kinetics exhibiting intermediates during folding (3,5,6,(11)(12)(13)(14)(15)(16). We address this problem here with the design of new FBP28 WW domain mutants and by examining their structural properties and folding kinetics.Because of the small size, fast folding kinetics, and biological importance, the formation of intermolecular β-sheets is thought to be a crucial event in the initiation and propagation of amyloid diseases, such as Alzheimer's disease, and spongiform encephalopathy, FBP28, and other WW domain proteins (e.g., Pin1 and FiP35) have been the subjects of extensive experimental (4,11,(17)(18)(19)(20)(21)(22)(23) and theoretical (3,5,6,(12)(13)(14)(15)(16)(24)(25)(26)(27) studies. However, a folding mechanism of the FBP28 was debatable for a long time because of its complexity.…”
mentioning
confidence: 99%